ArticleInfection and immunity2004
Glycosylation of the major polar tube protein of Encephalitozoon hellem, a microsporidian parasite that infects humans.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed.
- Article
- Cryo-ET reveals the in situ architecture of the polar tube invasion apparatus from microsporidian parasites.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NcPTP2, a polar tube protein, interacts with spore wall protein in the parasitic microsporidian Nosema ceranae.Molecular biology reports · 2024Article
- Ultrastructural insights into the microsporidian infection apparatus reveal the kinetics and morphological transitions of polar tube and cargo during host cell invasion.PLoS biology · 2024Article
- The microsporidian polar tube: origin, structure, composition, function, and application.Parasites & vectors · 2023Review
- Germination of Microsporidian Spores: The Known and Unknown.Journal of fungi (Basel, Switzerland) · 2023Review
- Identification and localization of polar tube proteins in the extruded polar tube of the microsporidian Anncaliia algerae.Scientific reports · 2023Article
- Article
- The Function and Structure of the Microsporidia Polar Tube.Experientia supplementum (2012) · 2022Article
- Mechanics of Microsporidian Polar Tube Firing.Experientia supplementum (2012) · 2022Article
- Genome and Evolutionary Analysis ofFrontiers in microbiology · 2021Article
- Identification and characterization a novel polar tube protein (NbPTP6) from the microsporidian Nosema bombycis.Parasites & vectors · 2020Article
- Invasion of Host Cells by Microsporidia.Frontiers in microbiology · 2020Review
- An Ultrastructural Study of the Extruded Polar Tube of Anncaliia algerae (Microsporidia).The Journal of eukaryotic microbiology · 2020Article
- Article
- Therapeutic targets for the treatment of microsporidiosis in humans.Expert opinion on therapeutic targets · 2018Review
- Microsporidia: Obligate Intracellular Pathogens Within the Fungal Kingdom.Microbiology spectrum · 2017Review
- The role of microsporidian polar tube protein 4 (PTP4) in host cell infection.PLoS pathogens · 2017Article
- Conjugation of Lectin to Poly(ε-caprolactone)-block-glycopolymer Micelles for In Vitro Intravesical Drug Delivery.Polymers · 2016Article
- Discovery of a Natural Microsporidian Pathogen with a Broad Tissue Tropism in Caenorhabditis elegans.PLoS pathogens · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The microsporidia are ubiquitous, obligate intracellular eukaryotic spore-forming parasites infecting a wide range of invertebrates and vertebrates, including humans. The defining structure of microsporidia is the polar tube, which forms a hollow tube through which the sporoplasm is transferred to the host cell. Research on the molecular and cellular biology of the polar tube has resulted in the identification of three polar tube proteins: PTP1, PTP2, and PTP3. The major polar tube protein, PTP1, accounts for at least 70% of the mass of the polar tube. In the present study, PTP1 was found to be posttranslationally modified. Concanavalin A (ConA) bound to PTP1 and to the polar tube of several different microsporidia species. Analysis of the glycosylation of Encephalitozoon hellem PTP1 suggested that it is modified by O-linked mannosylation, and ConA binds to these O-linked mannose residues. Mannose pretreatment of RK13 host cells decreased their infection by E. hellem, consistent with an interaction between the mannosylation of PTP1 and some unknown host cell mannose-binding molecule. A CHO cell line (Lec1) that is unable to synthesize complex-type N-linked oligosaccharides had an increased susceptibility to E. hellem infection compared to wild-type CHO cells. These data suggest that the O-mannosylation of PTP1 may have functional significance for the ability of microsporidia to invade their host cells.
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